Aggrecanase- and matrix metalloproteinase-mediated aggrecan degradation is associated with different molecular characteristics of aggrecan and separated in time ex vivo

References

• Behrens F, Kraft EL, Oegema TR Jr. (1989). Biochemical changes in articular cartilage after joint immobilization by casting or external fixation. J Orthop Res 7:335–43.
   PubMed Web of Science ®Google Scholar
• Caterson B, Flannery CR, Hughes CE, Little CB. (2000). Mechanisms involved in cartilage proteoglycan catabolism Matrix Biol 19:333–44.
   PubMed Web of Science ®Google Scholar
• Felson DT, Neogi T. (2004). Osteoarthritis: is it a disease of cartilage or of bone? Arthritis Rheum 50:341–4.
   PubMed Web of Science ®Google Scholar
• Flannery CR, Lark MW, Sandy JD. (1992). Identification of a stromelysin cleavage site within the interglobular domain of human aggrecan. Evidence for proteolysis at this site in vivo in human articular cartilage. J Biol Chem 267:1008–14.
   PubMed Web of Science ®Google Scholar
• Fosang AJ, Last K, Gardiner P, Jackson DC, Brown L. (1995). Development of a cleavage-site-specific monoclonal antibody for detecting metalloproteinase-derived aggrecan fragments: detection of fragments in human synovial fluids. Biochem J 310:337–43.
   PubMed Web of Science ®Google Scholar
• Fosang AJ, Last K, Maciewicz RA. (1996). Aggrecan is degraded by matrix metalloproteinases in human arthritis. Evidence that matrix metalloproteinase and aggrecanase activities can be independent. J Clin Invest 98:2292–9.
   PubMed Web of Science ®Google Scholar
• Fosang AJ, Last K, Stanton H, Weeks DB, Campbell IK, Hardingham TE, Hembry RM. (2000). Generation and novel distribution of matrix metalloproteinase-derived aggrecan fragments in porcine cartilage explants. J Biol Chem 275:33027–37.
   PubMed Web of Science ®Google Scholar
• Glasson SS, Askew R, Sheppard B, Carito B, Blanchet T, Ma HL, Flannery CR, Peluso D, Kanki K, Yang Z, Majumdar MK, Morris EA. (2005). Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis. Nature 434:644–8.
   PubMed Web of Science ®Google Scholar
• Hardingham TE, Fosang AJ. (1995). The structure of aggrecan and its turnover in cartilage. J Rheumatol Suppl 43:86–90.
   PubMedGoogle Scholar
• Ilic MZ, Haynes SR, Winter GM, Handley CJ. (1995). Kinetics of release of aggrecan from explant cultures of bovine cartilage from different sources and from animals of different ages. Acta Orthop Scand Suppl 266:33–7.
   PubMedGoogle Scholar
• Karsdal MA, Madsen SH, Christiansen C, Henriksen K, Fosang AJ, Sondergaard BC. (2008). Cartilage degradation is fully reversible in the presence of aggrecanase but not matrix metalloproteinase activity. Arthritis Res Ther 10:R63.
   PubMed Web of Science ®Google Scholar
• Karsdal MA, Sumer EU, Wulf H, Madsen SH, Christiansen C, Fosang AJ, Sondergaard BC. (2007). Induction of increased cAMP levels in articular chondrocytes blocks matrix metalloproteinase-mediated cartilage degradation but not aggrecanase-mediated cartilage degradation. Arthritis Rheum 56:1549–58.
   PubMed Web of Science ®Google Scholar
• Kiani C, Chen L, Wu YJ, Yee AJ, Yang BB. (2002). Structure and function of aggrecan. Cell Res 12:19–32.
   PubMed Web of Science ®Google Scholar
• Lark MW, Bayne EK, Flanagan J, Harper CF, Hoerrner LA, Hutchinson NI, Singer II, Donatelli SA, Weidner JR, Williams HR, Mumford RA, Lohmander LS. (1997). Aggrecan degradation in human cartilage. Evidence for both matrix metalloproteinase and aggrecanase activity in normal osteoarthritic and rheumatoid joints. J Clin Invest 100:93–106.
   PubMed Web of Science ®Google Scholar
• Little CB, Flannery C R, Hughes CE, Mort JS, Roughley PJ, Dent C, Caterson B. (1999). Aggrecanase versus matrix metalloproteinases in the catabolism of the interglobular domain of aggrecan in vitro. Biochem J 344:61–8.
   PubMed Web of Science ®Google Scholar
• Lohmander S, Antonopoulos CA, Friberg U. (1973). Chemical and metabolic heterogeneity of chondroitin sulfate and keratin sulfate in guinea pig cartilage and nucleus pulposus. Biochim Biophys Acta 304:430–48.
   PubMed Web of Science ®Google Scholar
• Maehara H, Suzuki K, Sasaki T, Oshita H, Wada E, Inoue T, Shimizu K. (2007). G1-G2 aggrecan product that can be generated by M-calpain on truncation at Ala709-Ala710 is present abundantly in human articular cartilage. J Biochem 141:469–77.
   PubMed Web of Science ®Google Scholar
• Malfait AM, Liu RQ, Ijiri K, Komiya S, Tortorella MD. (2002). Inhibition of ADAM-TS4 and ADAM-TS5 prevents aggrecan degradation in osteoarthritic cartilage. J Biol Chem 277:22201–8.
   PubMed Web of Science ®Google Scholar
• Mercuri FA, Maciewicz RA, Tart J, Last K, Fosang AJ. (2000). Mutations in the interglobular domain of aggrecan alter matrix metalloproteinase and aggrecanase cleavage patterns. Evidence that matrix metalloproteinase cleavage interferes with aggrecanase activity. J Biol Chem 275:33038–45.
   PubMed Web of Science ®Google Scholar
• Mok SS, Masuda K, Hauselmann HJ, Aydelotte MB, Thonar EJ. (1994). Aggrecan synthesized by mature bovine chondrocytes suspended in alginate. Identification of two distinct metabolic matrix pools. J Biol Chem 269:33021–7.
   PubMed Web of Science ®Google Scholar
• Oshita H, Sandy JD, Suzuki K, Akaike A, Bai Y, Sasaki T, Shimizu K. (2004). Mature bovine articular cartilage contains abundant aggrecan that is C-terminally truncated at Ala719-Ala720 a site which is readily cleaved by m-calpain. Biochem J 382:253–9.
   PubMed Web of Science ®Google Scholar
• Pratta MA, Tortorella MD, Arner EC. (2000). Age-related changes in aggrecan glycosylation affect cleavage by aggrecanase. J Biol Chem 275:39096–102.
   PubMed Web of Science ®Google Scholar
• Roughley PJ, Lee ER. (1994). Cartilage proteoglycans: structure and potential functions. Microsc Res Tech 28:385–97.
   PubMed Web of Science ®Google Scholar
• Rousseau JC, Sumer EU, Hein G, Sondergaard BC, Madsen SH, Pedersen C, Neumann T, Mueller A, Qvist P, Delmas P, Karsdal MA. (2008). Patients with rheumatoid arthritis have an altered circulatory aggrecan profile. BMC Musculoskelet Disord 9:74.
   PubMed Web of Science ®Google Scholar
• Sandy JD. (2006). A contentious issue finds some clarity: on the independent and complementary roles of aggrecanase activity and MMP activity in human joint aggrecanolysis. Osteoarthritis Cartilage 14:95–100.
   PubMed Web of Science ®Google Scholar
• Sandy JD, Flannery CR, Neame PJ, Lohmander LS. (1992). The structure of aggrecan fragments in human synovial fluid. Evidence for the involvement in osteoarthritis of a novel proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain. J Clin Invest 89:1512–16.
   PubMed Web of Science ®Google Scholar
• Sondergaard BC, Henriksen K, Wulf H, Oestergaard S, Schurigt U, Brauer R, Danielsen I, Christiansen C, Qvist P, Karsdal MA. (2006a). Relative contribution of matrix metalloproteinase and cysteine protease activities to cytokine-stimulated articular cartilage degradation. Osteoarthritis Cartilage 14:738–48.
   PubMed Web of Science ®Google Scholar
• Sondergaard BC, Wulf H, Henriksen K, Schaller S, Oestergaard S, Qvist P, Tanko LB, Bagger YZ, Christiansen C, Karsdal MA. (2006b). Calcitonin directly attenuates collagen type II degradation by inhibition of matrix metalloproteinase expression and activity in articular chondrocytes. Osteoarthritis Cartilage 14:759–68.
   PubMed Web of Science ®Google Scholar
• Stanton H, Rogerson FM, East CJ, Golub SB, Lawlor KE, Meeker CT, Little CB, Last K, Farmer PJ, Campbell IK, Fourie AM, Fosang AJ. (2005). ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro. Nature 434:648–52.
   PubMed Web of Science ®Google Scholar
• Struglics A, Larsson S, Pratta MA, Kumar S, Lark MW, Lohmander LS. (2006). Human osteoarthritis synovial fluid and joint cartilage contain both aggrecanase- and matrix metalloproteinase-generated aggrecan fragments. Osteoarthritis Cartilage 14:101–13.
   PubMed Web of Science ®Google Scholar
• Sumer EU, Sondergaard BC, Rousseau JC, Delmas PD, Fosang AJ, Karsdal MA, Christiansen C, Qvist P. (2007). MMP and non-MMP-mediated release of aggrecan and its fragments from articular cartilage: a comparative study of three different aggrecan and glycosaminoglycan assays. Osteoarthritis Cartilage 15:212–21.
   PubMed Web of Science ®Google Scholar
• Sztrolovics R, White RJ, Roughley PJ, Mort JS. (2002). The mechanism of aggrecan release from cartilage differs with tissue origin and the agent used to stimulate catabolism. Biochem J 362:465–72.
   PubMed Web of Science ®Google Scholar
• Tortorella M, Pratta M, Liu RQ, Abbaszade I, Ross H, Burn T, Arner E. (2000). The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage. J Biol Chem 275:25791–7.
   PubMed Web of Science ®Google Scholar
• Tortorella MD, Burn TC, Pratta MA, Abbaszade I, Hollis JM, Liu R, Rosenfeld SA, Copeland RA, Decicco CP, Wynn R and others. (1999). Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins. Science 284:1664–6.
   PubMed Web of Science ®Google Scholar